Research workbench
Crystal structure of cameline peptidoglycan recognition protein at 2.8A resolution
Analyse Crystal structure of cameline peptidoglycan recognition protein at 2.8A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R90
- Type
- protein
- Length
- 684 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidoglycan recognition protein
- UniProt
- Q9GK12
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Peptidoglycan recognition protein | protein | 171 | 26% helix, 20% strand | Q9GK12 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1090 | 0.84 | 0.85 | 117 | empty |
| 2 | 51 | 0.25 | 0.73 | 15 | empty |
| 3 | 52 | 0.25 | 0.72 | 16 | empty |
Interfaces
5 interfaces between chains.
- A–B · 779 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 539 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 374 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 105 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 75 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 2R90 · Crystal structure of cameline peptidoglycan recognition protein at 2.8A resolution · the same entry in another collection · chain A against A, TM-score 1.00
- Q9GK12 · AlphaFold monomer V2.0 prediction for peptidoglycan recognition protein 1 (Q9GK12) · a predicted model of the same protein · chain A against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9GK12
- Elsewhere: RCSB PDB 2R90 · PDBe 2R90 · UniProt Q9GK12
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